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Aedes aegypti kynurenine aminotransferase

Analyse Aedes aegypti kynurenine aminotransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1YIY
Type: protein
Length: 836 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Kynurenine aminotransferase
EC: 2.6.1.7, 2.6.1.64
UniProt: Q95VY4
Ligands: PMP, BR
Pockets: 11 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Kynurenine aminotransferase (EC 2.6.1.7, 2.6.1.64)	protein	418	45% helix, 15% strand	Q95VY4

Ligands and binding sites

PMP · 4'-deoxy-4'-aminopyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
BR · Bromide ion · ion · 5 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	361	0.77	0.87	56	PMP
2	504	0.75	0.83	76	PMP
3	72	0.64	0.91	21	empty
4	211	0.60	0.81	30	empty
5	105	0.47	0.80	21	empty

Interfaces

1 interface between chains.

A–B · 3094 Å² buried · 36 hydrogen bonds · protein-protein

Compared structures

1YIY · Aedes aegypti kynurenine aminotransferase · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q95VY4
Elsewhere: RCSB PDB 1YIY · PDBe 1YIY · UniProt Q95VY4

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